Sampietro T, Lenzi S, Cecchetti P, Giampietro O, Cruschelli L, Navalesi R
Clin Chem. 1986 Jul;32(7):1328-31.
Human platelet membrane proteins (PMP), incubated in vitro in the presence of various concentrations of glucose, undergo nonenzymatic glycation, as evidenced by incorporation of [3-3H]glucose radioactivity into the acid-precipitable fraction. The time course of the reaction is linear for the first hours, and the rate of glycation depends on the glucose concentration in the medium: at a glucose concentration of 80 mmol/L, up to 60 nmol of glucose is bound per milligram of PMP. The ketoaminic nature of the glucose/protein linkages was demonstrated by the finding of 5-hydroxymethylfurfuraldehyde by liquid-chromatographic analysis of acid hydrolysates of PMP. We analyzed PMP from 13 subjects with type I poorly controlled diabetes and from 10 nondiabetics. Nonenzymatic glycation, evaluated as nanomoles of the aldehyde per milligram of protein, was much greater in diabetic patients than in nondiabetics: 1.58 +/- 0.70 vs 0.37 +/- 0.18 (mean +/- SD).
在不同浓度葡萄糖存在的情况下于体外孵育的人血小板膜蛋白（PMP）会发生非酶糖基化，这可通过将[3-³H]葡萄糖放射性掺入酸沉淀部分得到证明。反应的时间进程在最初几个小时呈线性，糖基化速率取决于培养基中的葡萄糖浓度：在葡萄糖浓度为80 mmol/L时，每毫克PMP可结合多达60 nmol的葡萄糖。通过对PMP酸水解产物进行液相色谱分析发现5-羟甲基糠醛，证实了葡萄糖/蛋白质键的酮胺性质。我们分析了13名I型糖尿病控制不佳患者和10名非糖尿病患者的PMP。以每毫克蛋白质中醛的纳摩尔数评估的非酶糖基化，在糖尿病患者中比在非糖尿病患者中要高得多：分别为1.58±0.70和0.37±0.18（平均值±标准差）。
